ID   PANC_THEMA              Reviewed;         280 AA.
AC   Q9X0G6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Pantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_00158};
DE            Short=PS {ECO:0000255|HAMAP-Rule:MF_00158};
DE            EC=6.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00158};
DE   AltName: Full=Pantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00158};
DE   AltName: Full=Pantoate-activating enzyme {ECO:0000255|HAMAP-Rule:MF_00158};
GN   Name=panC {ECO:0000255|HAMAP-Rule:MF_00158};
GN   OrderedLocusNames=TM_1077;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in
CC       an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC       {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP +
CC         diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00158};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong
CC       mechanism. {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00158}.
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DR   EMBL; AE000512; AAD36154.1; -; Genomic_DNA.
DR   PIR; E72296; E72296.
DR   RefSeq; NP_228883.1; NC_000853.1.
DR   RefSeq; WP_004080408.1; NZ_CP011107.1.
DR   PDB; 2EJC; X-ray; 2.40 A; A=1-280.
DR   PDBsum; 2EJC; -.
DR   AlphaFoldDB; Q9X0G6; -.
DR   SMR; Q9X0G6; -.
DR   STRING; 243274.TM_1077; -.
DR   PaxDb; 243274-THEMA_08970; -.
DR   EnsemblBacteria; AAD36154; AAD36154; TM_1077.
DR   KEGG; tma:TM1077; -.
DR   eggNOG; COG0414; Bacteria.
DR   InParanoid; Q9X0G6; -.
DR   OrthoDB; 9773087at2; -.
DR   UniPathway; UPA00028; UER00005.
DR   EvolutionaryTrace; Q9X0G6; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IBA:GO_Central.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IBA:GO_Central.
DR   CDD; cd00560; PanC; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.30.1300.10; Pantoate-beta-alanine ligase, C-terminal domain; 1.
DR   HAMAP; MF_00158; PanC; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR003721; Pantoate_ligase.
DR   InterPro; IPR042176; Pantoate_ligase_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   NCBIfam; TIGR00018; panC; 1.
DR   PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1.
DR   PANTHER; PTHR21299:SF1; PANTOATE--BETA-ALANINE LIGASE; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis; Reference proteome.
FT   CHAIN           1..280
FT                   /note="Pantothenate synthetase"
FT                   /id="PRO_0000128280"
FT   ACT_SITE        37
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         61
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         61
FT                   /ligand="beta-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57966"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         147..150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         153
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         184..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           7..19
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           35..47
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   STRAND          48..55
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           68..70
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           75..83
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   STRAND          88..91
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           95..98
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           124..139
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   STRAND          142..147
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           151..163
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   STRAND          169..173
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           186..190
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           193..198
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           201..214
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   HELIX           220..232
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   STRAND          237..246
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   TURN            247..249
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   STRAND          260..268
FT                   /evidence="ECO:0007829|PDB:2EJC"
FT   STRAND          271..279
FT                   /evidence="ECO:0007829|PDB:2EJC"
SQ   SEQUENCE   280 AA;  32757 MW;  0BD1E4C572197163 CRC64;
     MRIIETIEEM KKFSEEMREK KKTIGFVPTM GYLHEGHLSL VRRARAENDV VVVSIFVNPT
     QFGPNEDYER YPRDFERDRK LLEKENVDCI FHPSVEEMYP PDFSTYVEET KLSKHLCGRS
     RPGHFRGVCT VVTKLFNIVK PHRAYFGQKD AQQFRVLRRM VRDLNMDVEM IECPIVREPD
     GLAMSSRNVY LSPEERQQAL SLYQSLKIAE NLYLNGERDA EKIKEEMIKH LSRFDKVKID
     YVEIVDEETL EPVEKIDRKV IVAVAAWVGN ARLIDNTILG
//